Binding of fibronectin to Clq; inhibition of binding by aggregated IgG.
Fibronectin was shown to bind to C1q using alkaline phosphatase conjugated fibronectin and C1q coated polystyrene tubes. The binding of the alkaline phosphatase conjugated fibronectin to C1q was dose dependent and inhibited by fibronectin and by the sulfated polymers heparin and chondroitin sulfate. The fibronectin interaction was inhibited only slightly by gelatin indicating that the fibronectin-gelatin interaction was different from that with C1q. Heat aggregated IgG blocked the binding of fibronectin to C1q and fibronectin inhibited the binding of aggregated IgG to C1q. These results suggest that fibronectin may be a factor affecting the determination of immune complexes in serum specimens by C1q binding assays.
D000469:Alkaline Phosphatase / Q000494:pharmacology; D000818:Animals; D000936:Antigen-Antibody Complex; D001665:Binding Sites; D001667:Binding, Competitive; D002809:Chondroitin Sulfates / Q000494:pharmacology; D003166:Complement Activating Enzymes; D015922:Complement C1q; D005353:Fibronectins / Q000378:metabolism*; D006493:Heparin / Q000494:pharmacology; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism*; D011817:Rabbits
D000936:Antigen-Antibody Complex; D005353:Fibronectins; D007074:Immunoglobulin G; D015922:Complement C1q; D006493:Heparin; D002809:Chondroitin Sulfates; D003166:Complement Activating Enzymes; D000469:Alkaline Phosphatase